ID   HSP60_PARBA             Reviewed;         592 AA.
AC   O60008; C1HBB8;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Heat shock protein 60, mitochondrial;
DE   AltName: Full=60 kDa chaperonin;
DE   AltName: Full=Protein Cpn60;
DE   Flags: Precursor;
GN   Name=HSP60; ORFNames=PAAG_08059;
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=12054056; DOI=10.1080/mmy.39.5.445.455;
RA   Salem-Izacc S.M., Gomez F.J., Jesuino R.S.A., Fonseca C.A., Felipe M.S.S.,
RA   Deepe G.S., de Almeida Soares C.M.;
RT   "Molecular cloning, characterization and expression of the heat shock
RT   protein 60 gene from the human pathogenic fungus Paracoccidioides
RT   brasiliensis.";
RL   Med. Mycol. 39:445-455(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- FUNCTION: May participate in assembly and/or disassembly of proteins
CC       imported into the mitochondrion. HSP60 are ATPases and have affinity
CC       for unfolded proteins (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR   EMBL; AF059523; AAC14712.1; -; Genomic_DNA.
DR   EMBL; KN294020; EEH37641.1; -; Genomic_DNA.
DR   RefSeq; XP_002789992.1; XM_002789946.2.
DR   AlphaFoldDB; O60008; -.
DR   SMR; O60008; -.
DR   STRING; 502779.O60008; -.
DR   PRIDE; O60008; -.
DR   EnsemblFungi; EEH37641; EEH37641; PAAG_08059.
DR   GeneID; 9093251; -.
DR   KEGG; pbl:PAAG_08059; -.
DR   VEuPathDB; FungiDB:PAAG_08059; -.
DR   eggNOG; KOG0356; Eukaryota.
DR   HOGENOM; CLU_016503_3_0_1; -.
DR   OMA; TDTDKME; -.
DR   OrthoDB; 415781at2759; -.
DR   Proteomes; UP000002059; Partially assembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   CDD; cd03344; GroEL; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   HAMAP; MF_00600; CH60; 1.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR   InterPro; IPR001844; Cpn60/GroEL.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Direct protein sequencing; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Stress response; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..592
FT                   /note="Heat shock protein 60, mitochondrial"
FT                   /id="PRO_0000005042"
SQ   SEQUENCE   592 AA;  62133 MW;  A90CCC826B5138ED CRC64;
     MQRAFTSSRA SVLSSASSTR APLSRFRSAG VGLQQQRFAH KELKFGVEAR ASLLKGIDTL
     AKAVTTTLGP KGRNVLIESP YGSPKITKDG VTVAKAVTLQ DKFENLGARL LQDVASKTNE
     VAGDGTTTAT VLARAIFSET VKNVAAGCNP MDLRRGIQSA VEAVVEYLQT NKRDITTTEE
     IAQVATISAN GDTHVGKLIS NAMEKVGKEG VITVKDGKTI DDELEVTEGM RFDRGYVSPY
     FITDTKAQKV EFEKPLILLS EKKISAVQDI IPALEASTSL RRPLVIIAED IEGEALAVCI
     LNKLRGQLQV AAVKAPGFGD NRKSILGDIG ILTNATVFTD ELDLKLEKAT PDMLGSTGSI
     TITKEDTIIL NGEGSKDAIA QRCEQIRSVI SDPATSDYEK EKLQERLAKL SGGVAVIKVG
     GASEIEVGEK KDRVVDALNA TRAAVEEGIL PGGGTALLKA AANGLTSLNP TNFDQKLGIS
     IIKNAITRPA RTIVENSGLE GSVIVGKLTD DFAGDFNRGF DSARGEYVDM IGAGIVDPLK
     VVRTALVDAS GVASLLGTTE VAIVEAPEEK VPAGSGAGGM GGGMGGMGGG MF